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DESCRIBE <http://purl.uniprot.org/SHA-384/26D475E2DBC0308CF336A0227C82664E936D768B0D5BF36B0BA47DAB01F23AC89AEFF05E623A24B2634E94F1B567DCA9>
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http://purl.uniprot.org/SHA-384/26D475E2DBC0308CF336A0227C82664E936D768B0D5BF36B0BA47DAB01F23AC89AEFF05E623A24B2634E94F1B567DCA9
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/26D475E2DBC0308CF336A0227C82664E936D768B0D5BF36B0BA47DAB01F23AC89AEFF05E623A24B2634E94F1B567DCA9
http://www.w3.org/2000/01/rdf-schema#comment
"These results suggest that transfer of the N-terminal acidic extension of HCII to alpha1-PI M358R enhanced its inhibition of thrombin by conferring the ability to bind exosite 1 on HAPI M358R."
xsd:string
http://purl.uniprot.org/uniprot/#_E70C091E3FF41BF7DBFD41A8FC9CA001CACDC4B30A4AAACA3A4CC23FF8D93DC73E01BDE7448E5D89D9249435FB7D2D83
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/26D475E2DBC0308CF336A0227C82664E936D768B0D5BF36B0BA47DAB01F23AC89AEFF05E623A24B2634E94F1B567DCA9
http://purl.uniprot.org/uniprot/P05546
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/26D475E2DBC0308CF336A0227C82664E936D768B0D5BF36B0BA47DAB01F23AC89AEFF05E623A24B2634E94F1B567DCA9
http://purl.uniprot.org/uniprot/#_P05546-mappedCitation-16981704
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/26D475E2DBC0308CF336A0227C82664E936D768B0D5BF36B0BA47DAB01F23AC89AEFF05E623A24B2634E94F1B567DCA9